ArticleMolecular and cellular biochemistry2018
Rv0646c, an esterase from M. tuberculosis, up-regulates the host immune response in THP-1 macrophages cells.
Article in Molecular and cellular biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 8 citations in OpenAlex.
- Roles of Lipolytic enzymes inFrontiers in microbiology · 2024Review
- Advanced phosphocreatine-grafted chitosan hydrogel promote wound healing by macrophage modulation.Frontiers in bioengineering and biotechnology · 2023Article
- LipG a bifunctional phospholipase/thioesterase involved in mycobacterial envelope remodeling.Bioscience reports · 2018Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
The genome sequence of Mycobacterium tuberculosis revealed the presence of several hydrolases involved in lipid metabolism including the members of Lip gene family. Rv0646c (LipG) is one of them. It is annotated as putative esterase/lipase because of the presence of consensus sequence 'GXSXG.' The gene was cloned, expressed, and purified in E. coli. It showed 22 U/mg specific activity with pNP-butyrate as a preferred substrate. However, it actively worked on substrates with short chain. The enzyme was optimally active at 50 °C/pH 8.0 and also stable up to 50 °C and in a lower pH range (pH 6-8). The K
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